Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline acetyl-CoA Identifier CHEBI:57288 (Beilstein: 8468140) help_outline Charge -4 Formula C23H34N7O17P3S InChIKeyhelp_outline ZSLZBFCDCINBPY-ZSJPKINUSA-J SMILEShelp_outline CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 352 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline streptothricin D Identifier CHEBI:60829 Charge 5 Formula C31H63N12O10 InChIKeyhelp_outline WUJTXMVGXDQPNN-OTQKCRDJSA-S SMILEShelp_outline [H][C@]12N\C(N[C@]1([H])C(=O)NC[C@H]2O)=[NH+]/[C@@H]1O[C@H](CO)[C@H](OC(N)=O)[C@@H](O)[C@H]1NC(=O)C[C@@H]([NH3+])CCCNC(=O)C[C@@H]([NH3+])CCCNC(=O)C[C@@H]([NH3+])CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,500 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline Nβ-acetylstreptothricin D Identifier CHEBI:141396 Charge 4 Formula C33H64N12O11 InChIKeyhelp_outline WPMGFKKSCCXUAK-YFZUDYRPSA-R SMILEShelp_outline [C@@H]1([C@@H]([C@@H]([C@H]([C@H](O1)CO)OC(N)=O)O)NC(C[C@@H](NC(=O)C)CCCNC(=O)C[C@H](CCCNC(C[C@@H]([NH3+])CCC[NH3+])=O)[NH3+])=O)/[NH+]=C/2\N[C@@]3(C(NC[C@H]([C@]3(N2)[H])O)=O)[H] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:57004 | RHEA:57005 | RHEA:57006 | RHEA:57007 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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In Bacillus subtilis, the SatA (formerly YyaR) acetyltransferase detoxifies streptothricin via lysine acetylation.
Burckhardt R.M., Escalante-Semerena J.C.
Soil is a complex niche, where survival of microorganisms is at risk due to the presence of antimicrobial agents. Many microbes chemically modify cytotoxic compounds to block their deleterious effects. Streptothricin is a broad-spectrum antibiotic produced by streptomycetes that affects Gram-posit ... >> More
Soil is a complex niche, where survival of microorganisms is at risk due to the presence of antimicrobial agents. Many microbes chemically modify cytotoxic compounds to block their deleterious effects. Streptothricin is a broad-spectrum antibiotic produced by streptomycetes that affects Gram-positive and Gram-negative bacteria alike. Here we identify the SatA (for <u>s</u>treptothricin <u>a</u>ce<u>t</u>yltransferase <u>A</u>, formerly YyaR) enzyme of <i>Bacillus subtilis</i> as the mechanism used by this soil bacterium to detoxify streptothricin. <i>B. subtilis</i> strains lacking <i>satA</i> were susceptible to streptothricin. Ectopic expression of <i>satA</i><sup>+</sup> restored streptothricin resistance to <i>B. subtilis</i><i>satA</i> (<i>Bs</i>SatA) strains. Purified <i>Bs</i>SatA acetylated streptothricin <i>in vitro</i> at the expense of acetyl-coenzyme A (acetyl-CoA). A single acetyl moiety transferred onto streptothricin by SatA blocked the toxic effects of the antibiotic. SatA bound streptothricin with high affinity (<i>K<sub>d</sub></i> [dissociation constant] = 1 μM), and did not bind acetyl-CoA in the absence of streptothricin. Expression of <i>B. subtilis</i><i>satA</i><sup>+</sup> in <i>Salmonella enterica</i> conferred streptothricin resistance, indicating that SatA was necessary and sufficient to detoxify streptothricin. Using this heterologous system, we showed that the SatA homologue from <i>Bacillus anthracis</i> also had streptothricin acetyltransferase activity. Our data highlight the physiological relevance of lysine acetylation for the survival of <i>B. subtilis</i> in the soil.<b>IMPORTANCE</b> Experimental support is provided for the functional assignment of gene products of the soil-dwelling bacilli <i>Bacillus subtilis</i> and <i>Bacillus anthracis</i> This study focuses on one enzyme that is necessary and sufficient to block the cytotoxic effects of a common soil antibiotic. The enzyme alluded to is a member of a family of proteins that are broadly distributed in all domains of life but poorly studied in <i>B. subtilis</i> and <i>B. anthracis</i> The initial characterization of the enzyme provides insights into its mechanism of catalysis. << Less
Appl. Environ. Microbiol. 83:E01590-E01590(2017) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.